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Publication Abstract from PubMed

Mitochondrial complex I powers ATP synthesis by oxidative phosphorylation, exploiting the energy from ubiquinone reduction by NADH to drive protons across the energy-transducing inner membrane. Recent cryo-EM analyses of mammalian and yeast complex I have revolutionized structural and mechanistic knowledge and defined structures in different functional states. Here, we describe a 2.7-A-resolution structure of the 42-subunit complex I from the yeast Yarrowia lipolytica containing 275 structured water molecules. We identify a proton-relay pathway for ubiquinone reduction and water molecules that connect mechanistically crucial elements and constitute proton-translocation pathways through the membrane. By comparison with known structures, we deconvolute structural changes governing the mammalian 'deactive transition' (relevant to ischemia-reperfusion injury) and their effects on the ubiquinone-binding site and a connected cavity in ND1. Our structure thus provides important insights into catalysis by this enigmatic respiratory machine.

Mitochondrial complex I structure reveals ordered water molecules for catalysis and proton translocation.,Grba DN, Hirst J Nat Struct Mol Biol. 2020 Aug 3. pii: 10.1038/s41594-020-0473-x. doi:, 10.1038/s41594-020-0473-x. PMID:32747785^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.